ID A0A094GB96_9PEZI Unreviewed; 2009 AA.
AC A0A094GB96;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=F-box domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=V500_03770 {ECO:0000313|EMBL:KFY93330.1};
OS Pseudogymnoascus sp. VKM F-4518 (FW-2643).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420913 {ECO:0000313|EMBL:KFY93330.1, ECO:0000313|Proteomes:UP000029284};
RN [1] {ECO:0000313|EMBL:KFY93330.1, ECO:0000313|Proteomes:UP000029284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4518 (FW-2643) {ECO:0000313|Proteomes:UP000029284};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC ECO:0000256|PROSITE-ProRule:PRU01023}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY93330.1}.
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DR EMBL; JPKC01001177; KFY93330.1; -; Genomic_DNA.
DR STRING; 1420913.A0A094GB96; -.
DR HOGENOM; CLU_001755_0_0_1; -.
DR Proteomes; UP000029284; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProt.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023270; RCMT_NCL1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22808:SF1; RNA CYTOSINE C(5)-METHYLTRANSFERASE NSUN2; 1.
DR Pfam; PF00646; F-box; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02011; RCMTNCL1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000029284};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01023};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01023};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 68..116
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT DOMAIN 1043..1456
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1509..1612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..577
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1535..1550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1339
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 1162..1168
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 1229
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 1256
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 1286
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 2009 AA; 218945 MW; D10534886288C919 CRC64;
MPSPSLKQAR RKRANPIAIV SNKGPWSQWH DPNSIEINSP PPTTSAAMSS ADPIAAPEAG
KAEQTPRSLT FLDLPSETQN AIMEQCTSSD LTSLSLVSKH FRDLAAAQIY SCFHIIFPDD
DDSTYESDRD GLAGGLNTMV TSDYDYARYL KDISLETVSG GAKGERAYRQ YTSDVSCGKF
MNTLFLLTLR KAKALETFSW DVRVELSRPV YKSLHSIPAL KHLYLRMHSG SSLYQKPPPL
PSLKCFPDDT MEVAKKIAKA AGGRSKAPPM KMTNAEAKAI LAPLAKDLKT DHAPTISGFK
NLKTLSILDM DSLEYIKEIK TSIHNSSSTL KKLQLSFSEA LARKARKPPP AADDTGDESD
QEIDEFGNMI PPPPVVAPSS IDDSSGPAKA FRAVEAKQAQ EAVLAQIFGI ESKPKDAGLA
RSDSNNEEKK SATGMEDTVN AFIKDFAALS KKVMGAPSSS ELTPEQKVFM KAVEKGARKY
LKGKKGALGG NSAKDGSEED SAGSSTEKVT PSSSSDTSDA GKADEEEKLS SAEPEYVGLF
DNEGKKDPKA HQSTDSPQPE DIDVCEPAEP EVESDSQDDD GPAPKLAAEE TTNDTQDAED
GAGSLVAEEA ANDAIPTTAA ESTDQSKVAK LVPGEKFHRD ILELALATRA LEGFRFHHLE
VDSLEYNVIK EAAEVHNRSL EKKDNSMSEY VRTTRGLTLR SLYIYLIPIK TSVLSRAVDL
HVLERISLLN VGPQAPLWNY LAKENKVSPL PLCKIHTDNV TVHFLKFVNQ LENLEELFIL
ERSTKSSEYS FAPKTTVTTD NIRRYVLKKH ASSLMRLVIK NENDYTWDAN VKFLELLCRQ
GKKLTELGIS FASPALHTFN QYLPGLVSLE ALHIINFRND DTCHWVMREV PRFIADSLSS
HPGMKLEYLA LGNTVGRLVR KLKVVPKPKD KGKGKATMYT GNTIIISEEK PDESESDEED
VSAPGLNLET VECGRFYDIP HSAAATTWLG GRGGGRGKGR GGGGGRDSRD NRVSYDKIDK
TNEKFERYYN SIIELPEEER AQFWAALRRD LPNSFRFAGS KGHALAVQKQ LRERYIPEIT
KIEHYDGTAV EAPKPVPWYP DELAWWMTTP KNVVRRFPPF AAFQKYLVSE TSVGNISRQE
VVSMIPPLLM GIEPGMTVLD MCAAPGSKAA QLLEMVHKGE EARIRNALRL HAKEDGREIS
PGLDVVGDED LNVDSEDFGR ATGLLIANDS DYKRSHMLIH QLKRLSSPNL IVTNHDATIF
PSIKLPPTKE DPAQNRYLKF DRILADVPCS GDGTCRKNPN LWQDWSPSNA LGLYVTQVRI
LVRALQMLKA GGRVVYSTCS MNPVENEAVI ASAIERCGGL EKVQLIDCSD QLVGLKRKEG
LKQWTIMDKS GKVWEDWPSV DAENQKNGSN PATARLAEGM FTPTGEAAKI PLERCMRVYA
HQQDTGGFFI TVLQKMTEFK AKPESEARKS EPKPAIISIV EEIEAQPAPA PGANVAPKIE
AADLLEGSTS TDLEDQNVPA VARENQASDK PDATLPAKRA FDDSDVAPSS PKKAKIESNG
SEVEALSLDR QVHFPPPPGA ELDATIRPGD LRPETTPATT TSLPAPVKAK GRNQQQFEEP
FKYISGDHPE VQSIDEFYKL SQRFPRDRFM VRNALGEPAK TIYYTSALIR DILVENEGKG
IKFIHGGVRM FMKQDVQGEG VCRWRIQSEG MPILEGYVGE GRVVRLYKRS TLRKLLIEMF
PKVTDGCWKE LGEIGERVRD IGMGCCVLRI EPSDEEGGFK ERIVLPLWRS LHSLNLMLAK
EDRTAMLLRI FNENVPLVNN HHPSQRAAAV VDAAVAEAEV AEAETANGNG DAVVEKSEGV
EMDAAEAPLE SEAASDQLIV AAYSVNSTTT TAPTTCSDPA TPSLAAAPSP VEEGNVVKSS
VEDVDSVRRG VACGGGGVPV ILGVDAAGTD AVLAVVAAAV DAFGVYGAVL GRGAAAGAVR
AAGIGGEDAA VAAGFVARGA VALEDVAGG
//
